Studies suggest that Matrixyl, also known as Palmitoyl pentapeptide-4 and Palmitoyl pentapeptide-3, seems to have a structure distinct from other pentapeptides due to its conjugation with palmitoyl. This structural change is thought to improve its transport throughout the skin and reinforce its stability against enzymatic destruction by skin proteases, leading to possibly more revitalized skin cells.
Research suggests that the synthetic nature of Matrixyl and the hope that it may increase collagen formation in the skin are at the core of its appeal. It has been hypothesized that Matrixyl, a matrikine, may have a role in cell activity coordination via interactions with certain receptors. Wrinkles and fine lines are often thought to result from a decline in collagen, the structural protein responsible for the skin’s firmness and elasticity. Matrixyl’s potential to boost collagen production may help restore skin’s elasticity, investigations purport.
Scientists speculate this lipopeptide is interesting since it is a synthetic isomer of fatty and amino acids. In this definition, an isomer is a molecule structurally similar to another molecule but has a distinct set of atomic building blocks. Matrixyl contains a micro-collagen peptide responsible for the substance’s purported effects.
This page delves into the science behind Matrixyl, including its mode of action, current studies, and prospects.
Matrixyl Peptide: Mechanism of Action
Recent research suggests that the Matrixyl peptide may be potent in the context of skin-remodeling, with potential properties for wound healing and the complex mechanisms behind wrinkle generation. It was uncovered due to parallel lines of inquiry in the field of dermatology: the hunt for a way to speed up the recovery time after skin wounds.
Matrixyl, like copper peptides, is thought to work by inciting the skin’s deeper “matrix” layers to begin the healing process. Fibroblasts, specialized cells, are thought to play a crucial part in this system by helping heal skin wounds. The ability of fibroblasts to produce collagen declines with age, which is thought to contribute to the aging-related slowing of wound healing.
Findings have implied that Matrixyl’s potential to stimulate these fibroblasts into renewing their production of collagen and fibronectin, two crucial building blocks of skin, is only one of its unique features. Matrixyl seems able to fight this natural part of aging due to its potential impact on fibroblasts.
Matrixyl Peptide and Collagen Synthesis
Researchers nowadays are interested in Matrixyl because of its potential as a signal peptide fragment of the C-terminal propeptide of type I collagen. This peptide is thought to “stimulate feedback regulation of new collagen synthesis and ECM proteins” by sending signals to fibroblasts.
Connective tissue cells, known as fibroblasts, are essential to creating and maintaining the extracellular matrix (ECM), a network of proteins and carbohydrates that gives tissues and organs their shape and function. Collagens, elastins, fibronectins, and laminins are essential proteins that make up the ECM and help tissues maintain their structures. The tensile strength of these structures comes from collagen, the fundamental structural protein. Fibroblasts play a major role in wound restoration by laying down new collagen fibers to replace dead or dying tissue.
The critical aggregation concentration is thought to be related to Matrixyl’s concentration-dependent activity in stimulating collagen formation, suggesting a relationship between self-assembly and collagen production. Hydrogen bonds, electrostatic forces, hydrophobic interactions, aromatic bonding (- blending), and van der Waals forces are all involved in this self-assembly process. These complex pathways suggest why Matrixyl may have great potential for promoting fibroblast regeneration.
Matrixyl Peptide and Scar Size
Matrixyl’s possible impact on fibroblast contractility and its potential function in scar formation were examined in a notable study.
Results suggested that Matrixyl may successfully suppress -SMA (alpha-smooth muscle actin) expression and prevent fibroblasts from transforming into myofibroblasts. The protein -SMA is characteristic of smooth muscle cells, including those lining blood arteries and other organs, including the gastrointestinal and urinary tract. Myofibroblasts, specialized cells essential to wound healing and tissue repair, also express this.
Increased production of -SMA by myofibroblasts is associated with excessive collagen deposition and scar tissue development in fibrotic scarring. The possibility that Matrixyl might regulate these processes offers promise for managing scars and accelerating wound healing.
Matrixyl Peptides and Tissue
The potential of Matrixyl in accelerating wound closure was studied in an animal study. Animals were diverged into seven groups and were observed for 21 days as part of the research. Good results were speculated in groups exposed to greater quantities of Matrixyl than a control group, suggesting that Matrixyl may have a good impact on wound healing. Macroscopic data suggested improvements ranging from 63.5% to 81.81% in the experimental groups, compared to the negative control group, suggesting a probable significant augmentation in wound healing.
Scientists interested in further studying this peptide are encouraged to click here to be redirected to Core Peptides’ website for the highest quality research compounds and most educational scientific papers.
References:
[i] Choi, Y. L., Park, E. J., Kim, E., Na, D. H., & Shin, Y. H. (2014). Dermal Stability and In Vitro Skin Permeation of Collagen Pentapeptides (KTTKS and palmitoyl-KTTKS). Biomolecules & therapeutics, 22(4), 321–327. https://doi.org/10.4062/biomolther.2014.053
[ii] MatrixylTM https://inci.guide/peptides/matrixyltm
[iii] Errante, F., Ledwoń, P., Latajka, R., Rovero, P., & Papini, A. M. (2020). Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Frontiers in chemistry, 8, 572923. https://doi.org/10.3389/fchem.2020.572923
[iv] Jones, R. R., Castelletto, V., Connon, C. J., & Hamley, I. W. (2013). Collagen stimulating effect of peptide amphiphile C16-KTTKS on human fibroblasts. Molecular pharmaceutics, 10(3), 1063–1069. https://doi.org/10.1021/mp300549d
[v] Park H, An E, Cho Lee AR. Effect of Palmitoyl-Pentapeptide (Pal-KTTKS) on Wound Contractile Process in Relation with Connective Tissue Growth Factor and α-Smooth Muscle Actin Expression. Tissue Eng Regen Med. 2017 Jan 19;14(1):73-80. https://link.springer.com/article/10.1007/s13770-016-0017-y
